Table I. Known Splicing Factors/Snrnps/Saps Identified in Functional Spliceosomes

Table I. Known Splicing Factors/Snrnps/Saps Identified in Functional Spliceosomes

Table I. Known splicing factors/snRNPs/SAPs identified in functional spliceosomes.

The GenBank accession number for each protein is presented with a clickable link to the protein sequence and to the SWISS-PROT (representative peptides matched to MS/MS spectra from AdML spliceosomes are highlighted in red). # of pep. iden. refers to the number of filtered unique MS/MS spectra that match to the corresponding protein. Abbreviations and motifs (obtained from NCBI Conserved Domain Database): SAP, spliceosome-associated protein; SGD, saccharomyces genome database (Stanford, CA); COLD, cold shock RNA binding domain; Cyclophilin, cyclophilin type peptidyl-prolyl cis-trans isomerase; DExD, DExD/H-like helicases superfamily; FF, contains two conserved F residues, often accompanies WW domains; G domain, GTP binding domain that contains a P-loop motif; GYF, contains conserved G-T-F residues; HAT, Half-A-TPR (tetratrico-peptide repeat); HELICc, helicase superfamily c-terminal domain; KH, hnRNP K homology RNA-binding domain; MIF4G, middle domain of eukaryotic initiation factor 4G; NOP, putative snoRNA binding domain; PABP, poly-adenylate binding protein, unique domain; PP2A, protein phosphatase 2A repeat; PWI, domain in splicing factors; RED, protein with extensive stretch of alternating R and E or D; RRM, RNA recognition motif (RRM, RBD, or RNP domain); RS, RS domain found in SR or SR-related splicing factors; SKIP, conserved domain found in chromatinic proteins; Sm, snRNP Sm proteins; SWAP, suppressor-of-white-apricot splicing regulator; TUDOR, domain present in several RNA-binding proteins; TyrKc, tyrosine kinase, catalytic domain; UBQ, ubiquitin homologues; WD40s, WD40 repeats, structural repeats (blades) of the beta propeller domain; WW, domain with 2 conserved W residues, binds proline-rich polypeptides; ZF, Zinc finger domain.

Table II. Proteins newly identified in functional spliceosomes.

Yeast homologs were identified based on high sequence similarity to their human counterparts and are indicated by *. Abbreviations and Motifs: fSAP, functional spliceosome-associated protein; DEATH, domain found in proteins involved in cell death; DSRM, double-stranded RNA binding motif; ERM, ezrin/radixin/moesin family motif; HP, hypothetical protein; NUDIX, mutT-like domain; Ubox, modified RING finger domain. See Table I for additional footnotes and motifs.

Table III. Proteins designated as H complex components.

List of proteins found in the spliceosomes but not designated as spliceosome components because the Table III proteins are abundant in the non-specific H complex. For abbreviations, see footnotes for Tables I and II.